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Identification of a Novel Glycosaminoglycan Core-like Molecule I

Adriana, Manzi and Salimath, P. V. and Robert, C. Spiro and Keifer, Paul A. (1995) Identification of a Novel Glycosaminoglycan Core-like Molecule I. Journal of Biological Chemistry, 270 (16). pp. 9154-9163.

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Abstract

Beta-Xylosides compete with endogenous proteoglycan core proteins and act as alternate acceptors for synthesizing protein-free glycosaminoglycan chains. Their assembly on these alternate acceptors utilizes the same glycosyltransferases that make the protein-bound chains. Most studies using alternate acceptors focus on the production of sulfated glycosaminoglycan chains that are thought to be the major products. However, we previously showed that labeling melanoma cells with [6-H]galactose in the presence of 4-methylumbelliferyl (MU) or p-nitrophenyl (pNP) -xylosides led to the synthesis of mostly di- to tetrasaccharide products including incomplete core structures. We have solved the structure of one of the previously unidentified products as, GalNAc (1, 4) GlcA (1, 3) Gal (1, 3) Gal (1, 4) XylMU, based on compositional analysis by high performance liquid chromatography, fast atom bombardment, electrospray mass spectrometry, and one-dimensional and two-dimensional H NMR spectroscopy. The novel aspect of this molecule is the presence of a terminal -GalNAc residue at a position that is normally occupied by -GalNAc in chondroitin/dermatan sulfate or by -GlcNAc in heparin or heparan sulfate chains. An -GalNAc residue at this critical location may prevent further chain extension or influence the type of chain subsequently added to the common tetrasaccharide core.

Item Type: Article
Uncontrolled Keywords: glycosaminoglycan Beta-Xylosides
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 16 Protein Biochemistry
Divisions: Biochemistry and Nutrition
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 09 Jan 2008 06:39
Last Modified: 28 Dec 2011 09:32
URI: http://172.16.1.6/id/eprint/1621

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